ID A0A2S0JCU3_CAMFE Unreviewed; 348 AA. AC A0A2S0JCU3; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 03-MAY-2023, entry version 17. DE SubName: Full=Type II asparaginase {ECO:0000313|EMBL:AVK81266.1}; DE EC=3.5.1.1 {ECO:0000313|EMBL:AVK81266.1}; GN Name=ansB {ECO:0000313|EMBL:AVK81266.1}; GN ORFNames=C6B32_05305 {ECO:0000313|EMBL:AVK81266.1}; OS Campylobacter fetus subsp. testudinum. OC Bacteria; Pseudomonadota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1507806 {ECO:0000313|EMBL:AVK81266.1, ECO:0000313|Proteomes:UP000240030}; RN [1] {ECO:0000313|EMBL:AVK81266.1, ECO:0000313|Proteomes:UP000240030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=772 {ECO:0000313|EMBL:AVK81266.1, RC ECO:0000313|Proteomes:UP000240030}; RA Hou S.; RT "Complete Genome Sequence of Campylobacter fetus subsp. testudinum Strain RT 772, isolated from ascites of patient with peritonitis."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the asparaginase 1 family. CC {ECO:0000256|ARBA:ARBA00010518, ECO:0000256|RuleBase:RU004456}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP027287; AVK81266.1; -; Genomic_DNA. DR RefSeq; WP_058909345.1; NZ_WLYB01000004.1. DR AlphaFoldDB; A0A2S0JCU3; -. DR STRING; 1244528.CFT03427_1004; -. DR EnsemblBacteria; AVK81266; AVK81266; C6B32_05305. DR OrthoDB; 9788068at2; -. DR Proteomes; UP000240030; Chromosome. DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt. DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro. DR CDD; cd08964; L-asparaginase_II; 1. DR Gene3D; 3.40.50.40; -; 1. DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1. DR InterPro; IPR004550; AsnASE_II. DR InterPro; IPR036152; Asp/glu_Ase-like_sf. DR InterPro; IPR006034; Asparaginase/glutaminase-like. DR InterPro; IPR020827; Asparaginase/glutaminase_AS1. DR InterPro; IPR027475; Asparaginase/glutaminase_AS2. DR InterPro; IPR040919; Asparaginase_C. DR InterPro; IPR027473; L-asparaginase_C. DR InterPro; IPR027474; L-asparaginase_N. DR InterPro; IPR037152; L-asparaginase_N_sf. DR PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1. DR PANTHER; PTHR11707; L-ASPARAGINASE; 1. DR Pfam; PF00710; Asparaginase; 1. DR Pfam; PF17763; Asparaginase_C; 1. DR PIRSF; PIRSF001220; L-ASNase_gatD; 1. DR PIRSF; PIRSF500176; L_ASNase; 1. DR PRINTS; PR00139; ASNGLNASE. DR SMART; SM00870; Asparaginase; 1. DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 1. DR TIGRFAMs; TIGR00520; asnASE_II; 1. DR PROSITE; PS00144; ASN_GLN_ASE_1; 1. DR PROSITE; PS00917; ASN_GLN_ASE_2; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AVK81266.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..348 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015552509" FT DOMAIN 24..215 FT /note="L-asparaginase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00710" FT DOMAIN 235..345 FT /note="Asparaginase/glutaminase C-terminal" FT /evidence="ECO:0000259|Pfam:PF17763" FT ACT_SITE 32 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10099" FT ACT_SITE 32 FT /note="O-isoaspartyl threonine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR001220-1" FT ACT_SITE 111 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2" FT BINDING 111..112 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2" SQ SEQUENCE 348 AA; 37395 MW; 32903C360C2965D9 CRC64; MCLIKKVFIL MLITMSAMFA KPTIYILATG GTIAGSSASS LSSGYTSGTV TVDKLISAVP QINEIATIKG EQISNIGSQE MNNDVWLKLA KRVNELLDSK NVDGIVITHG TDTMEETAYF LNLVVKSDKP IVMVGAMRNS DSLSSDGPLN LYNAVNVAMS KDAVGKGVLV VMNDEIHAAR EITKTNTTSV DTFKSPNTGK IGTVIYGNVK FYMQSTRKHT KNSEFDISTI SSLPRVDIIF SHSNDNPDFV NAAVKNGAKG IINAGMGNGN IYPSALEALA KAVKQGVIVV RDSRVGSGET TNPGEIDDAK YGFLTSDNLN AQKARVLLMV ALTKTSDPKK IEEYFLTY //